The relation between cytoarchitecture and the biochemistry and regulation of gene expression are studied. Polyribosomes appear attached to microtrabeculae in extracted cell skeletons by mRNA. mRNP proteins serve as skeletal components Poliovirus and VSV infection reorganize the cytoskeleton. Host mRNA is released, viral mRNA attached and the intermediate filament region modified for viral replication and assembly. The extracted cytoskeleton is covered by a plasma lamina derived from the plasma membrane and contains 80% of the intact cell surface proteins measured by iodination, lectin and virus binding sites and by scanning microscopy. This protein sheet retains much of intact cell morphology and appears an integral part of the cytoskeleton. Fusing myoblasts have an unstable plasma lamina in fusion regions which becomes stabilized and retains acetylcholine receptor in the myotube. The hnRNP has been visualized as a fiber network in extracted nuclei. New techniques visualize the selectively stained network in whole nuclei using HV microscopy. Drug induced morphological and biochemical changes are studied. mRNA enters the cytoplasm attached to the cytoskeleton. Its movement to the cell periphery is followed by autoradiography. Control of gene expression is studied in suspended and reattached anchorage dependent fibroblasts. mRNA is reversibly modified to untranslatability in suspended cells. Untranslatable "message" sequences are found to comprize much post-polysomal Poly(A) plus RNA in all cells. Protein synthesis is triggered by cell contact to a surface without cell spreading. Later phases of cell recovery from suspension are studied by varying cell shape with controlled adhesivity surfaces. Cell response to suspension depends on degree of "transformation" and is studied in a transformed cell series. Cell configuration controls specific structural gene protein expression. Prolonged suspension superinduces gamma actin synthesis - 58K intermediate filament message is translated in flat cells but not in suspended. Tubulin message production is controlled by free tubulin level.